Reviewed, UniProtKB/Swiss-Prot P15636 (API_ACHLY)

Names and origin

Protein names	Recommended name:     Protease 1     EC=3.4.21.50 Alternative name(s):     Protease I     API     Lysyl endopeptidase
Organism	Achromobacter lyticus
Taxonomic identifier	224 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Achromobacter

Protein attributes

Sequence length	653 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.
Subcellular location	Secreted.
Domain	The C-terminal extension has little effect on the function of API.
Post-translational modification	Three disulfide bonds are present.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 PKD domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Or 27 Potential

Propeptide

21 – 205

185

Ref.2

PRO_0000028515

Chain

206 – 473

268

Protease 1

PRO_0000028516

Propeptide

474 – 653

180

Thr/Ser-rich

PRO_0000028517

Regions

Domain

474 – 553

80

PKD

Sites

Active site

262

1

Charge relay system By similarity

Active site

318

1

Charge relay system By similarity

Active site

399

1

Charge relay system By similarity

Amino acid modifications

Disulfide bond

211 ↔ 421

Ref.2

Disulfide bond

217 ↔ 285

Disulfide bond

241 ↔ 263

Secondary structure

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653

Helix Strand Turn

Details...

Helix

218 – 220

3

Helix

226 – 229

4

Beta strand

230 – 235

6

Beta strand

238 – 246

9

Beta strand

256 – 260

5

Helix

261 – 263

3

Helix

268 – 272

5

Beta strand

275 – 277

3

Helix

291 – 294

4

Beta strand

304 – 306

3

Beta strand

308 – 314

7

Turn

315 – 318

4

Beta strand

319 – 326

8

Helix

330 – 332

3

Beta strand

335 – 337

3

Beta strand

349 – 353

5

Helix

355 – 357

3

Beta strand

361 – 365

5

Beta strand

370 – 372

3

Beta strand

376 – 378

3

Beta strand

380 – 386

7

Beta strand

402 – 404

3

Beta strand

410 – 416

7

Helix

425 – 427

3

Beta strand

428 – 434

7

Helix

435 – 440

6

Helix

445 – 447

3

Helix

450 – 453

4

Beta strand

461 – 463

3

Sequences

	Sequence		Length	Mass (Da)
	P15636-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 3A55159247EFFE7C	FASTA	653	68,125
	10 20 30 40 50 60 MKRICGSLLL LGLSISAALA APASRPAAFD YANLSSVDKV ALRTMPAVDV AKAKAEDLQR 70 80 90 100 110 120 DKRGDIPRFA LAIDVDMTPQ NSGAWEYTAD GQFAVWRQRV RSEKALSLNF GFTDYYMPAG 130 140 150 160 170 180 GRLLVYPATQ APAGDRGLIS QYDASNNNSA RQLWTAVVPG AEAVIEAVIP RDKVGEFKLR 190 200 210 220 230 240 LTKVNHDYVG FGPLARRLAA ASGEKGVSGS CNIDVVCPEG DGRRDIIRAV GAYSKSGTLA 250 260 270 280 290 300 CTGSLVNNTA NDRKMYFLTA HHCGMGTAST AASIVVYWNY QNSTCRAPNT PASGANGDGS 310 320 330 340 350 360 MSQTQSGSTV KATYATSDFT LLELNNAANP AFNLFWAGWD RRDQNYPGAI AIHHPNVAEK 370 380 390 400 410 420 RISNSTSPTS FVAWGGGAGT THLNVQWQPS GGVTEPGSSG SPIYSPEKRV LGQLHGGPSS 430 440 450 460 470 480 CSATGTNRSD QYGRVFTSWT GGGAAASRLS DWLDPASTGA QFIDGLDSGG GTPNTPPVAN 490 500 510 520 530 540 FTSTTSGLTA TFTDSSTDSD GSIASRSWNF GDGSTSTATN PSKTYAAAGT YTVTLTVTDN 550 560 570 580 590 600 GGATNTKTGS VTVSGGPGAQ TYTNDTDVAI PDNATVESPI TVSGRTGNGS ATTPIQVTIY 610 620 630 640 650 HTYKSDLKVD LVAPDGTVYN LHNRTGGSAH NIIQTFTKDL SSEAAQRAPG SCG

References

[1]	"Cloning, nucleotide sequence, and expression of Achromobacter protease I gene." Ohara T., Makino K., Shinagawa H., Nakata A., Norioka S., Sakiyama F. J. Biol. Chem. 264:20625-20631(1989) [PubMed: 2684982] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: M497-1.
[2]	"The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease." Tsunasawa S., Masaki T., Hirose M., Soejima M., Sakiyama F. J. Biol. Chem. 264:3832-3839(1989) [PubMed: 2492988] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-473, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 206-473. Strain: M497-1.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05128 Genomic DNA. Translation: AAA78946.1.

PIR

A32687.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ARB	X-ray	1.20	A	206-473	[»]
1ARC	X-ray	2.00	A	206-473	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.280.

Enzyme and pathway databases

BRENDA

3.4.21.50. 19051.

Family and domain databases

InterPro

IPR017323. Lysyl_endo-pept.
IPR000601. PKD.
IPR002884. PrprotnconvertsP.
[Graphical view]

Pfam

PF01483. P_proprotein. 1 hit.
PF00801. PKD. 1 hit.
[Graphical view]

PIRSF

PIRSF037930. Lysyl_endopeptidase. 1 hit.

SMART

SM00089. PKD. 1 hit.
[Graphical view]

PROSITE

PS50093. PKD. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

API_ACHLY

Accession

Primary (citable) accession number: P15636

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)